Structural Analysis of the Carboxyl Terminal Peptide From Human Chorionic Gonadotropin β-Subunit by Two-Dimensional Nuclear Magnetic Resonance Spectroscopy

Authors


B-237, HHMI, Beckman Center, Stanford, CA 94305-5428.

Abstract

PROBLEM: Vaccines that target human chorionic gonadotropin (hCG) might be made more effective through greater understanding of the solution three-dimensional structure and behavior of the hormone.

METHOD: A 37-amino acid carboxyl terminal peptide of the hCG beta subunit was synthesized, purified, and analyzed by two-dimensional nuclear magnetic resonance spectroscopy. RESULTS: Double-quantum filtered correlated spectroscopy data on the peptide in water at 4°C reveals 27 multiplets in the peptide fingerprint region, as expected. A nuclear Overhauser effect spectroscopy spectrum shows several intraresidual peaks in the amide region but lacks clearly assignable interresidual signals.

CONCLUSION: By itself in water the carboxyl terminal peptide of hCG lacks defined secondary structure elements and is thus likely a random coil. The presence of beta turns appears possible although neither their existence nor their localization can be confirmed.

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